کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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35899 | 45113 | 2007 | 5 صفحه PDF | دانلود رایگان |
A melibiose- and xylose-cospecific homodimeric lectin was isolated from fresh fruiting bodies of Boletus edulis. The lectin was isolated using a protocol that consisted of ion exchange chromatography on DEAE-cellulose, affinity chromatography on CM-cellulose and gel filtration by fast protein liquid chromatography on Superdex 75. It was a dimer made up of two 16.3 kDa subunits. The hemagglutinating activity of the lectin was stable up to 40 °C, and in the presence of NaOH or HCl solutions up to a concentration of 25 mM. The hemagglutinating activity of the lectin was unaffected in the presence of AlCl3 and FeCl3 at and above 2 mM. MgCl2, ZnCl2 and MnCl2 inhibited the lectin activity. The lectin stimulated the mitogenic response of mouse splenocytes attaining a maximum at 1 μM, and inhibited human immunodeficiency virus-1 reverse transcriptase with an IC50 of 14.3 μM. It did not exhibit antifungal activity.
Journal: Process Biochemistry - Volume 42, Issue 12, December 2007, Pages 1620–1624